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The enzymatic activity and function of a new α‐1,3‐glucosyltransferase, Cps18CU, derived from Streptococcus pneumoniae serotype 18C was identified for the first time using the enzymatically synthetic disaccharide Rhaβ1,4‐Glcα‐PP‐O(CH2)11‐OPh as the… Click to show full abstract
The enzymatic activity and function of a new α‐1,3‐glucosyltransferase, Cps18CU, derived from Streptococcus pneumoniae serotype 18C was identified for the first time using the enzymatically synthetic disaccharide Rhaβ1,4‐Glcα‐PP‐O(CH2)11‐OPh as the acceptor substrate. Further investigation on substrate specificity revealed that Cps18CU exhibited broad toleration toward various NDP‐Glc donors and also accepted such disaccharide acceptor containing Rhaβ1,4‐Glc moiety in structure. Finally, Cps18CU was employed into a one‐pot two‐enzyme reaction system, furnishing trisaccharide Glcα1,3‐Rhaβ1,4‐Glcα‐PP‐O(CH2)11‐OPh in an 81 % yield.
Journal Title: ChemCatChem
Year Published: 2021
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